ID   ETFA_SYNWW              Reviewed;         317 AA.
AC   Q0AZ33;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Electron transfer flavoprotein subunit alpha {ECO:0000303|PubMed:23468890};
GN   Name=etfA {ECO:0000303|PubMed:23468890};
GN   OrderedLocusNames=Swol_0697 {ECO:0000312|EMBL:ABI68021.1};
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=335541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen;
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INDUCTION, AND PATHWAY.
RX   PubMed=19648244; DOI=10.1128/jb.01605-08;
RA   Mueller N., Schleheck D., Schink B.;
RT   "Involvement of NADH:acceptor oxidoreductase and butyryl coenzyme A
RT   dehydrogenase in reversed electron transport during syntrophic butyrate
RT   oxidation by Syntrophomonas wolfei.";
RL   J. Bacteriol. 191:6167-6177(2009).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, SUBCELLULAR LOCATION,
RP   FUNCTION, AND PATHWAY.
RX   PubMed=23468890; DOI=10.1371/journal.pone.0056905;
RA   Schmidt A., Mueller N., Schink B., Schleheck D.;
RT   "A proteomic view at the biochemistry of syntrophic butyrate oxidation in
RT   Syntrophomonas wolfei.";
RL   PLoS ONE 8:E56905-E56905(2013).
CC   -!- FUNCTION: Part of an electron transfer flavoprotein involved in
CC       syntrophic growth of S.wolfei with butyrate. Probably receives
CC       electrons from butyryl-CoA dehydrogenases, and transfers them to the
CC       membrane-bound quinone oxidoreductase Swol_0698.
CC       {ECO:0000305|PubMed:19648244, ECO:0000305|PubMed:23468890}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P13804};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P13804};
CC   -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC       {ECO:0000305|PubMed:19648244, ECO:0000305|PubMed:23468890}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC       {ECO:0000250|UniProtKB:P13804}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23468890}.
CC   -!- INDUCTION: Highly expressed during syntrophic growth with butyrate (at
CC       protein level) (PubMed:19648244, PubMed:23468890). Seems to be
CC       constitutively expressed (PubMed:23468890).
CC       {ECO:0000269|PubMed:19648244, ECO:0000269|PubMed:23468890}.
CC   -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC       {ECO:0000305}.
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DR   EMBL; CP000448; ABI68021.1; -; Genomic_DNA.
DR   RefSeq; WP_011640126.1; NC_008346.1.
DR   AlphaFoldDB; Q0AZ33; -.
DR   SMR; Q0AZ33; -.
DR   STRING; 335541.Swol_0697; -.
DR   EnsemblBacteria; ABI68021; ABI68021; Swol_0697.
DR   KEGG; swo:Swol_0697; -.
DR   eggNOG; COG2025; Bacteria.
DR   HOGENOM; CLU_034178_0_1_9; -.
DR   OMA; LFVRPIY; -.
DR   OrthoDB; 1400253at2; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000001968; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01715; ETF_alpha; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR014730; ETF_a/b_N.
DR   InterPro; IPR001308; ETF_a/FixB.
DR   InterPro; IPR033947; ETF_alpha_N.
DR   InterPro; IPR014731; ETF_asu_C.
DR   InterPro; IPR018206; ETF_asu_C_CS.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR43153; PTHR43153; 1.
DR   Pfam; PF01012; ETF; 1.
DR   Pfam; PF00766; ETF_alpha; 1.
DR   PIRSF; PIRSF000089; Electra_flavoP_a; 1.
DR   SMART; SM00893; ETF; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   PROSITE; PS00696; ETF_ALPHA; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Electron transport; FAD; Fatty acid metabolism; Flavoprotein;
KW   Lipid metabolism; Reference proteome; Transport.
FT   CHAIN           1..317
FT                   /note="Electron transfer flavoprotein subunit alpha"
FT                   /id="PRO_0000442217"
SQ   SEQUENCE   317 AA;  33043 MW;  DB6786C4617D7239 CRC64;
     MAGTWIFVEQ RDGNIRKVTF EMLSEAKKFG DEVAAVVFGK GVEALAPEFA KYGADKVYVV
     EDDVFANYNT GAYVAQMVAM INEFKPNAVL FAHTFNGRDF ASRLAQKLQL GLATDAIKVE
     VSAGKGVFTR AIYAGKALAK VEVAGEPVLG TIRPGVCEVG NTAGAGAVVK PAVAATAADV
     YQTVKSFVPT VSARPELTEA DVVVSGGRGC KGPDGIKLVE QLADLLGAAV GGSRASIDSG
     WLGHELQVGQ TGKVVNPNLY VAAGISGAIQ HLAGMSSSKF IAAINTDTEA PIFNVSDFGV
     VADLFKVIPT LVSELKK